ID   PLMP_PLEOS              Reviewed;         168 AA.
AC   P81055;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Peptidyl-Lys metalloendopeptidase;
DE            Short=MEP;
DE            EC=3.4.24.20;
DE   AltName: Full=PoMEP;
GN   Name=MEP;
OS   Pleurotus ostreatus (Oyster mushroom) (White-rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Pleurotaceae; Pleurotus.
OX   NCBI_TaxID=5322;
RN   [1]
RP   PROTEIN SEQUENCE, AND MASS SPECTROMETRY.
RX   PubMed=9374478; DOI=10.1074/jbc.272.48.30032;
RA   Nonaka T., Dohmae N., Hashimoto Y., Takio K.;
RT   "Amino acid sequences of metalloendopeptidases specific for acyl-lysine
RT   bonds from Grifola frondosa and Pleurotus ostreatus fruiting bodies.";
RL   J. Biol. Chem. 272:30032-30039(1997).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-11, AND ACTIVITY REGULATION.
RX   PubMed=8541645; DOI=10.1271/bbb.59.2074;
RA   Dohmae N., Hayashi K., Miki K., Tsumuraya Y., Hashimoto Y.;
RT   "Purification and characterization of intracellular proteinases in
RT   Pleurotus ostreatus fruiting bodies.";
RL   Biosci. Biotechnol. Biochem. 59:2074-2080(1995).
RN   [3]
RP   SUBSTRATE SPECIFICITY.
RX   PubMed=9644258; DOI=10.1093/oxfordjournals.jbchem.a022074;
RA   Nonaka T., Hashimoto Y., Takio K.;
RT   "Kinetic characterization of lysine-specific metalloendopeptidases from
RT   Grifola frondosa and Pleurotus ostreatus fruiting bodies.";
RL   J. Biochem. 124:157-162(1998).
RN   [4]
RP   ACTIVITY REGULATION, ZINC-BINDING, AND COFACTOR.
RX   AGRICOLA=IND21804865;
RA   Choi H.-S., Shin H.-H.;
RT   "Purification and partial characterization of a fibrinolytic protease in
RT   Pleurotus ostreatus.";
RL   Mycologia 90:674-679(1998).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage in proteins: -Xaa-|-Lys- (in which Xaa
CC         may be Pro).; EC=3.4.24.20;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|Ref.4};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000269|Ref.4};
CC   -!- ACTIVITY REGULATION: Inhibited by chelating agents such as EDTA and
CC       1,10-phenanthroline. {ECO:0000269|PubMed:8541645, ECO:0000269|Ref.4}.
CC   -!- SUBCELLULAR LOCATION: Secreted. Note=Binds strongly to beta-1,3-glucan
CC       and chitin, major polysaccharides constituting the fungal cell wall.
CC       {ECO:0000250}.
CC   -!- MASS SPECTROMETRY: Mass=17927; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:9374478};
CC   -!- SIMILARITY: Belongs to the peptidase M35 family. {ECO:0000305}.
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DR   AlphaFoldDB; P81055; -.
DR   SMR; P81055; -.
DR   MEROPS; M35.004; -.
DR   VEuPathDB; FungiDB:PLEOSDRAFT_1037634; -.
DR   BRENDA; 3.4.24.20; 4912.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd11306; M35_peptidyl-Lys; 1.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR029463; Lys_MEP.
DR   InterPro; IPR034115; M35_peptidyl-Lys.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   Pfam; PF14521; Aspzincin_M35; 1.
DR   SMART; SM01351; Aspzincin_M35; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Hydrolase; Metal-binding;
KW   Metalloprotease; Protease; Secreted; Zinc.
FT   CHAIN           1..168
FT                   /note="Peptidyl-Lys metalloendopeptidase"
FT                   /id="PRO_0000078237"
FT   ACT_SITE        119
FT                   /evidence="ECO:0000250|UniProtKB:P81054"
FT   BINDING         118
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P81054"
FT   BINDING         122
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P81054"
FT   BINDING         131
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P81054"
FT   SITE            134
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   DISULFID        6..76
FT                   /evidence="ECO:0000250|UniProtKB:P81054"
FT   DISULFID        78..98
FT                   /evidence="ECO:0000250|UniProtKB:P81054"
SQ   SEQUENCE   168 AA;  17925 MW;  78E5556CB1566547 CRC64;
     ATFVGCSATR QTQLNAAASQ AQTYAANALS YLNSHTSSTT RYTTWFGTFV TSRYNTVLSH
     FSSISSNTFS SYTFDCTCSD SGTYAFVNPS NFGYVTLCGA FWNAPVAGTD SRGGTLIHES
     SHFTRNGGTD DHVYGQAGAQ SLARSNPAQA IDNADSHEYF AENNPALA